ID A0A080M6L5_9PROT Unreviewed; 714 AA.
AC A0A080M6L5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=RTX-I toxin determinant B {ECO:0000313|EMBL:KFB76898.1};
GN Name=apxIB_2 {ECO:0000313|EMBL:KFB76898.1};
GN ORFNames=AW06_002018 {ECO:0000313|EMBL:KFB76898.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB76898.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB76898.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFB76898.1}.
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DR EMBL; JDST02000041; KFB76898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M6L5; -.
DR STRING; 1453999.AW06_002018; -.
DR Proteomes; UP000021315; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd18783; ABC_6TM_PrtD_LapB_HlyB_like; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000021315};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..130
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 162..441
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 474..709
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 714 AA; 78179 MW; 9C467D9307D5B4EF CRC64;
MTEKFSHSVV QCLAAIAQNQ GIRINPERLI HDFALADEEP AAPLVLRMAA DIGMKAKADR
LTWSQLVAQQ GVFPVLGRLN SGAGVIVVGI RQEGESKQVA VVDPCAAAVA ITFYSEEAFG
AIWSGDVILL KKAHSIFDAQ QPFGLRWFIP EILKQRTAFR DVFIAGMAMN VLALASPLFF
QVVIDKVLVH QNASTLMVLT AGVIIAMLFD AAFGYLRQIL LLAATNKIDM HVTRRAFGHL
LSLSIDFFEL STAGVVTRQM QQLEGIRHFL TGRLLFAGMD ALALVIFLPL LFTYSFKLAL
IVLGFALIIA LIITILLPTF RKRLDRLNSA EGVRQALLVE TIHGMRTVKA LAIEPVQRKA
WDQLSAEAIN AHFQVGKLSI AGNLATEFLG KLMPVVIVFI GAQSIFDQTM SVGVLIAFQM
LSGRVINPLI QIVSLINEYQ QTAVSVRMLA EIMNRPPEGR IGAGGLRPLL KGQISFEEVT
FRYPGASVNA LDRTSFTIPA GAVVGVVGRS GSGKTTLTKL IQGLYPVQEG LVRFDGIDAR
EIDLSHLRRQ IGVVLQENFL FRGSIRDNLT ITKPDATIEE IVAAAQAAGA DEFIERMPQG
YDTLLEENAS NLSGGQKQRL SIARSLLARP NILILDEAAS ALDPESEAIF IRNLSRIAVG
RTVIMISHRL STLVNADVVL VMQNGRLSDW GTHTQLLSRC ETYQHLWNQQ TGHL
//
